The influence of temperature on glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase and the regulation of these enzymes in a mesophilic and a thermophilic cyanobacterium |
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Authors: | Henk J Lubberding Peter V M Bot |
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Institution: | (1) Biological Laboratory, Vrije Universiteit, De Boelelaan 1087, NL1081 HV Amsterdam, The Netherlands |
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Abstract: | The activities and kinetics of the enzymes G6PDH (glucose-6-phosphate dehydrogenase) and 6PGDH (6-phosphogluconate dehydrogenase) from the mesophilic cyanobacterium Synechococcus 6307 and the thermophilic cyanobacterium Synechococcus 6716 are studied in relation to temperature. In Synechococcus 6307 the apparent K
m's are for G6PDH: 80M (substrate) and 20M (NADP+); for 6PGDH: 90M (substrate) and 25M (NADP+). In Synechococcus 6716 the apparent K
m's are for G6PDH: 550M (substrate) and 30M (NADP+); for 6PGDH: 40M (substrate) and 10M (NADP+). None of the K
m's is influenced by the growth temperature and only the K
m's of G6PDH for G6P are influenced by the assay temperature in both organisms. The idea that, in general, thermophilic enzymes possess a lower affinity for their substrates and co-enzymes than mesophilic enzymes is challenged.Although ATP, ribulose-1,5-bisphosphate, NADPH and pH can all influence the activities of G6PDH and 6PGDH to a certain extent (without any difference between the mesophilic and the thermophilic strain), they cannot be responsible for the total deactivation of the enzyme activities observed in the light, thus blocking the pentose phosphate pathway.Abbreviations G6PDH
glucose-6-phosphate, dehydrogenase
- 6PGDH
6-phosphogluconate dehydrogenase
- G6P
glucose-6-phosphate
- 6PG
6-phosphogluconate
- RUDP
ribulose-1,5-bisphosphate
- Tricine
N-Tris (hydroxymethyl)-methylglycine |
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Keywords: | Cyanobacteria Synechococcus Synechocystis Thermophily Temperature effects Glucose-6-phosphate dehydrogenase 6-Phosphogluconate dehydrogenase Enzyme kinetics Enzyme regulation |
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